Abstract
The chromosomal gef gene of Escherichia coli is a member of the gef gene family which encodes strongly toxic proteins of about 50 amino acids. We demonstrate here that the Gef protein is detectable by anti-peptide antibodies. Furthermore, we show that Gef is anchored in the cytoplasmic membrane by the N-terminal part of the protein, and that the C-terminal part is localized in the periplasm in a dimeric form with at least one disulphide bond. By mutagenesis of gef it is shown that the periplasmic portion of Gef encodes the toxic domain and that the dimerization of Gef is not essential for the toxic effect.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Toxins / metabolism
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Base Sequence
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Blotting, Western
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Cell Membrane / chemistry
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DNA Mutational Analysis
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Escherichia coli / ultrastructure*
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Escherichia coli Proteins*
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Gene Expression
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Genes, Bacterial
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Macromolecular Substances
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Membrane Proteins*
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Molecular Sequence Data
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Multigene Family
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Mutagenesis, Site-Directed
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Plasmids / genetics
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Protein Conformation
Substances
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Bacterial Proteins
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Bacterial Toxins
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Escherichia coli Proteins
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Macromolecular Substances
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Membrane Proteins
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HokC protein, E coli